Literature summary for 1.4.3.3 extracted from

Dib, I.; Stanzer, D.; Nidetzky, B.
Trigonopsis variabilis D-amino aacid oxidase: control of protein quality and opportunities for biocatalysis through production in Escherichia coli (2007), Appl. Environ. Microbiol., 73, 331-333.

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	exogenous FAD (0.01 to 1 mM) added to assay or protein storage buffers does not enhance the catalytic activity of native and recombinant DAO	Trigonopsis variabilis

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Trigonopsis variabilis
expression in Escherichia coli. TvDAO can be produced in Escherichia coli as a fully functional recombinant protein. They also show that microheterogeneity due to modification of Cys108 is avoided completely during production and purification	Trigonopsis variabilis

General Stability

General Stability	Organism
oriented immobilization of a chimeric oxidase maintains 80% of the original activity in microparticle-bound enzymes. Mildly permeabilized cells in which N-terminally tagged TvDAO in which a 12-amino-acid peptide is fused in frame to the N-terminus (TvDAOstrepN) is physically entrapped are employed for the batchwise conversion of D-Ala in an aerated enzyme reactor. The cells could be reused for at least three rounds of reaction with only small losses of activity. The free enzyme, however, is rapidly inactivated under the same reaction conditions (half-life: 1.2 h)	Trigonopsis variabilis

Organism

oriented immobilization of a chimeric oxidase maintains 80% of the original activity in microparticle-bound enzymes. Mildly permeabilized cells in which N-terminally tagged TvDAO in which a 12-amino-acid peptide is fused in frame to the N-terminus (TvDAOstrepN) is physically entrapped are employed for the batchwise conversion of D-Ala in an aerated enzyme reactor. The cells could be reused for at least three rounds of reaction with only small losses of activity. The free enzyme, however, is rapidly inactivated under the same reaction conditions (half-life: 1.2 h)

Trigonopsis variabilis

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	resistant to the oxidants O2 and H2O2	Trigonopsis variabilis

Organism

Organism	UniProt	Comment	Textmining
Trigonopsis variabilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Trigonopsis variabilis
MonoQ column chromatography	Trigonopsis variabilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
cephalosporin C + H2O + O2	-	Trigonopsis variabilis	7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2	-	?
D-alanine + H2O + O2	-	Trigonopsis variabilis	pyruvate + NH3 + H2O2	-	?
D-methionine + H2O + O2	-	Trigonopsis variabilis	4-methylthio-2-oxobutanoic acid + NH3 + H2O2	-	?

Synonyms

Synonyms	Comment	Organism
D-amino acid oxidase	-	Trigonopsis variabilis
DAO	-	Trigonopsis variabilis
TvDAO	-	Trigonopsis variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	-	increasing the temperature to 30°C does not affect the specific activity but enhances the volumetric enzyme activity by 22% due to its effect on cell growth	Trigonopsis variabilis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Trigonopsis variabilis